Sandbox Reserved 1099

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{{Sandbox_ESBS_2019}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE -->
{{Sandbox_ESBS_2019}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE -->
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'''Dermcidin''' is a '''Human''' [https://en.wikipedia.org/wiki/Antimicrobial_peptides_ antimicrobial peptide] of 109 amino acids presents in sweat involved in the regulation of skin flora. This molecule encoded by the ''DCD gene'' plays a role in the host defense system and thus, is able to prevent microbial growth after injuries or any skin disorders.
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'''Dermcidin''' is a '''Human''' [https://en.wikipedia.org/wiki/Antimicrobial_peptides_ antimicrobial peptide] of 109 amino acids presents in sweat involved in the regulation of skin flora. This molecule encoded by the ''DCD gene'' plays a role in the host defense system as hexameric channel and thus, is able to prevent infection after injuries or any skin disorders.
== Expression and function ==
== Expression and function ==
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*[https://fr.wikipedia.org/wiki/Défensine_ Defensins] which are cationic peptides (α-defensins and β-defensins)
*[https://fr.wikipedia.org/wiki/Défensine_ Defensins] which are cationic peptides (α-defensins and β-defensins)
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Dermcidin gene is expressed as precursor only in mucous cells of eccrine sweat glands within the dermis of the skin and the derived-peptide is secreted by granules in sweat. The active also named DCD-1 form contains the end C-terminal from the 62 to the 109 residue and is probably created by proteases in sweat under specific conditions. The sweat is acidic and composed of salt concentration such as sodium, chloride, potassium and magnesium. The sweat is acidic and composed of
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Dermcidin gene is expressed as precursor only in mucous cells of eccrine sweat glands within the dermis of the skin and the derived-peptide is secreted by granules in sweat. The active form also named DCD-1 contains the end C-terminal from the 62 to the 109 residue and is probably created by proteases in sweat under specific conditions. The sweat is acidic and composed of salt concentration such as sodium, chloride, potassium and magnesium.
This form is involved in the [https://en.wikipedia.org/wiki/Innate_immune_system_ innate immune system] and protect from a variety of pathogenic microorganisms.
This form is involved in the [https://en.wikipedia.org/wiki/Innate_immune_system_ innate immune system] and protect from a variety of pathogenic microorganisms.
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== Structural highlights ==
== Structural highlights ==
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size, proteolytically processed
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size, proteolytically processed, helix-hinge-helix
== Antimicrobial activity ==
== Antimicrobial activity ==

Revision as of 17:25, 2 January 2020

This Sandbox is Reserved from 25/11/2019, through 30/9/2020 for use in the course "Structural Biology" taught by Bruno Kieffer at the University of Strasbourg, ESBS. This reservation includes Sandbox Reserved 1091 through Sandbox Reserved 1115.
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Dermcidin is a Human antimicrobial peptide of 109 amino acids presents in sweat involved in the regulation of skin flora. This molecule encoded by the DCD gene plays a role in the host defense system as hexameric channel and thus, is able to prevent infection after injuries or any skin disorders.

Contents

Expression and function

The gene DCD is located on the chromosome 12 and has no homology with other known antimicrobial peptides. Indeed, there are already two classes of mammalian antimicrobial peptides known :

Dermcidin gene is expressed as precursor only in mucous cells of eccrine sweat glands within the dermis of the skin and the derived-peptide is secreted by granules in sweat. The active form also named DCD-1 contains the end C-terminal from the 62 to the 109 residue and is probably created by proteases in sweat under specific conditions. The sweat is acidic and composed of salt concentration such as sodium, chloride, potassium and magnesium.

This form is involved in the innate immune system and protect from a variety of pathogenic microorganisms.

Structural highlights

size, proteolytically processed, helix-hinge-helix

Antimicrobial activity

Related disease

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</StructureSection>

References

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